Chapter 2

Chemistry Comes Alive

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Why Chemistry
• Human body organization begins with chemical
level
– Atoms
– Molecules

• Chemistry underlies all physiological reactions

– Movement, digestion, pumping of heart, nervous
system

• Study chemistry = understanding of physiological

functions

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Elements Atoms
• Atoms – basic structure of all things • Composed of three subatomic particles
– Protons – positively charged (+)
• All elements are made up of atoms

• Four elements make up 96% of the human – Neutrons – no charged

body
– Carbon (C) – Electrons – negatively charged (-)
– Oxygen (O)
– Hydrogen (H)
– Nitrogen (N)

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 Atoms Chemical Bonding
• Protons and neutrons are found in a • Most atoms chemically combine with other
centrally located nucleus atoms to form molecules
– Stable associations between two or more atoms
combined in a fixed ratio
• Electrons orbit around the nucleus – Atoms held together by chemical bonds

• Major types of chemical bonds

• Number of positive protons is balanced by – Ionic bonds
number of negative electrons, so atoms – Covalent bonds
are electrically neutral – Hydrogen bonds
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Chemical Bonds
Atoms
Ionic Bonds
• Isotopes • Attraction force between oppositely charged ions that
holding them together
– Structural variations of same atom containing
same number of protons but differ in the • Ions are atoms that either loss or gain an electron or
number of neutrons electrons

– Positive charged ions (cations) – atoms that loss electrons

• Radioisotopes are isotopes that emit • Na+, H+, K+, Ca2+

radiation energy as they decomposed to – Negative charged ions (anions) – atoms that gain electrons
more stable forms • Cl-, HCO3-
– This energy is referred to as radioactivity
• Formation of ionic compounds such as salt (NaCl –
table salt)
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Chemical Bonds
Atoms
Covalent Bonds
• Radioisotopes are a valuable tool for • Sharing of electrons between atoms
biological research and medicine – Strongest bond with highest energy content
– Share same chemistry as their stable isotopes so
will be taken up by body
– Can then be used for diagnosis of disease • Two types
– Non-polar covalent bonds – atoms shared
electrons equally
• All radioactivity can damage living tissue
– Polar covalent bonds – atoms shared
– Cause cancer
electrons unequally resulting in partially
– Used to destroy localized cancers – radiation charged molecules
therapy

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 Chemical Reactions
• Synthesis reactions
– Involve atoms or molecules combining to form
larger, more complex molecule
– Used in anabolic (building) processes

• Decomposition reactions
– Involve breakdown of a molecule into smaller
molecules or its constituent atoms (reverse of
synthesis reactions)
– Involve catabolic (bond-breaking) reactions

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Chemical Bonds
Hydrogen Bonds
• Weak attractions between partially
positive hydrogen of one molecule and a
partially negative atom of another
molecule

• Collectively important in
– How water behave
– Maintaining the shape of complex molecules
such as DNA and proteins

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Chemical Reactions
• All chemical reactions are either exergonic
or endergonic
– Exergonic reactions result in a net release of
energy (give off energy)
• Catabolic and oxidative reactions

– Endergonic reactions result in a net

absorption of energy (use up energy)
• Anabolic reactions

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 Water Properties of Water
• Composes two-thirds of the human body by • Reactivity
weight – Necessary part of hydrolysis and dehydration
synthesis reactions
• Most important for life because of its
properties
– High heat capacity • Cushioning
– High heat of vaporization – Protects certain organs from physical trauma
– Polar solvent properties • Example: cerebrospinal fluid cushions nervous
– Reactivity system organs
– Cushioning

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Properties of Water Salts

• High heat capacity • Salts are ionic compounds that dissociate
– Ability to absorb and release heat with little
into separate ions in water
temperature change – Separate into cations (positively charged
molecules) and anions (negatively charged)
– Prevents sudden changes in body – All ions are called electrolytes because they can
temperature conduct electrical currents in solution
– Ions play specialized roles in body functions
• Sodium, potassium, calcium
• High heat of vaporization – Ionic balance is vital for homeostasis
– Evaporation requires large amounts of heat – Common salts in body
– Useful cooling mechanism (sweating) • NaCl, CaCO3, KCl

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Properties of Water Acids and Bases

• Polar solvent properties • An acid dissociates in water to produce H+
– Dissolves and dissociates ionic substances – Also called a proton donor
– Important acids
– Forms hydration (water) layers around large • HCl (hydrochloric acid), HC2H3O2 (acetic acid,
charged molecules abbreviated HAc), and H2CO3 (carbonic acid)
• Example: proteins
– Body’s major transport medium • A base accepts H+ when added to solution
– Also called a proton acceptor
– Important bases
• Bicarbonate ion (HCO3–) and ammonia (NH3)

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 Acids and Bases Homeostatic Imbalance
pH is a measure of H+ in a
solution
• Enzymes in the body work within a very
• Expressed as a number between 0 and 14
narrow pH range
The pH of 7 is termed neutral
(pure water) • An arterial pH of 7.0 during
Acid has pH from 0 to < 7
cardiopulmonary resuscitation predicts a
poor outcome
• The lower the pH = stronger the acid

Base has pH > 7 to 14

• Patients presenting with an arterial pH of
• The higher the pH = stronger the base less than 6.85 rarely survive
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Biological Macromolecules
Acids and Bases
General Characteristics
• Neutralization reaction occurs when acids • Organic molecules – molecules that
and bases are mixed, returned to neutral, contain both carbon and hydrogen
forming water and salt
• Four classes of biomolecules in living
– Acids neutralized by adding base systems
• e.g., medications to neutralize stomach acid – Carbohydrates
containing base – Lipids
– Bases neutralized by adding acid – Proteins
– Nucleic acids

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Biological Macromolecules
Acids and Bases
General Characteristics
• Buffers are substances that help to resist • Polymers – molecules made up for
abrupt and large swing in pH repeating subunits termed monomers
– Carbonic acid (weak acid) and bicarbonate – Monomers identical or similar in chemical
(weak base) buffer system for blood pH structure
– Examples
• Carbohydrates with sugar monomers
• Nucleic acids with nucleotide monomers
• Proteins with amino acid monomers

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 Biological Macromolecules
Carbohydrates
General Characteristics
• Three classes
• Synthesized by dehydration synthesis – Monosaccharides – one single sugar
– Disaccharides – two sugars
– Polysaccharides – many sugars
• Broken down by hydrolysis reactions

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Carbohydrates
• Monosaccharides
– Simple sugars containing three to seven
carbon atoms
– Monomers of carbohydrates
– Important monosaccharides
• Pentose sugars – ribose and deoxyribose
• Hexose sugars – glucose (blood sugar), fructose,
galactose

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Carbohydrates Carbohydrates
• Includes sugars and starches • Disaccharides
– Two sugars bonded together
• Contains carbon (C), hydrogen (H), and – Too large to pass through cell membranes
oxygen (O)
– Formed by dehydration synthesis of two
monosaccharides
• Chemical formula is (CH2O)n – Important disaccharides
– n the number of carbon atoms • Sucrose (table sugar) – glucose and fructose
• Lactose (milk sugar) – glucose and galactose
• Major energy source for the body • Maltose (malt sugar) – glucose and glucose

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 Carbohydrates Lipids
• Polysaccharides • Triglycerides
– Polymers of monosaccharides – Called fats when solid and oils when liquid
• Formed by dehydration synthesis of many
monomers – Composed of three fatty acids (linear
– Important polysaccharides hydrocarbons) bonded to a glycerol molecule
• Starch – carbohydrate storage form used by
(sugar alcohol) by dehydration synthesis
plants – Main functions
• Glycogen – carbohydrate storage form used by • Energy storage
animals
• Insulation
– Not very soluble • Protection

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Lipids Lipids
• Contain C, H, O, but less than in • Triglycerides can be constructed of
carbohydrates, and sometimes contain P
• Insoluble in water – Saturated fatty acids
• Main types
– Triglycerides – Unsaturated fatty acids
– Phospholipids
– Steroids
– Eicosanoids

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 Lipids
• Triglycerides
– Saturated fatty acids
• All carbons are linked via single covalent bonds
• These create linear molecules which can pack
closely together forming a solid at room
temperature (animal fats, butter)

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Lipids
• Phospholipids
– Modified triglycerides
• Glycerol and two fatty acids plus a phosphorus-
containing group
– “Head” and “tail” regions have different
properties
• Head is polar and hydrophilic (attracted to water)
• Tails are nonpolar and hydrophobic (repelled by
water)
– Important in cell membrane structure

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Lipids
• Triglycerides
– Unsaturated fatty acids
• One or more carbons are linked via double bonds
• Double bonds cause a kink in the fatty acid so they
cannot pack together closely resulting in
unsaturated fatty acids being liquid at room
temperature (plant oils, such as olive oil)
• Omega-3 fatty acids – “heart healthy”
– Trans fats – modified unsaturated fatty oils
that resemble structure of saturated fats and
considered unhealthy
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 Lipids Proteins
• Steroids • Comprise 20–30% of cell mass
– Consist of four interlocking ring structures • Have most varied functions of any molecules
– Most important steroid is cholesterol – Structural, chemical (enzymes), contraction
(muscles)
• Made by liver and also found in animal products
(ex: cheese, eggs, meat) • Contain C, H, O, N, and sometimes S and P
– Starting material for synthesis of vitamin D, • Polymers of amino acid monomers held
steroid hormones, and bile salts together by peptide bonds
– Important in cell plasma membrane structure • Shape and function due to four structural
levels

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Lipids Proteins
• Eicosanoids • All proteins are made from 20 types of
– Derived from a fatty acid (arachidonic acid) amino acids
found in cell membranes – Joined by covalent bonds called peptide
– Most important eicosanoids are bonds
prostaglandins • Formed during dehydration synthesis reaction
• Play a role in blood clotting, control of blood • Occur between amine group of one amino acid
pressure, inflammation, and labor contractions and the carboxylic group of another
• Inflammatory actions are blocked by NSAIDs (non-
steroidal anti-inflammatory drugs, such as aspirin
or ibuprofen)

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 Protein Structures
• Proteins have two shapes
– Fibrous – strand-like, water-insoluble proteins
• Provide mechanical support and tensile strength
• Keratin, elastin, collagen

– Globular – compact, spherical, water-soluble,

extremely sensitive to environmental changes
• Antibodies, hormones, enzymes

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Protein Structure Protein Structure

• Four levels of protein structure determine • Denaturation – globular proteins unfold
shape and function and lose their functional 3-D shape
– Primary – linear sequence of amino acids
– Secondary – interaction of primary structure due • Can be caused by decreased pH
to hydrogen bonds (increased acidity) or increased
• Alpha helix – coils resemble a spring temperature
• Beta pleated sheets – resemble accordion ribbons
– Tertiary – interaction of secondary structure due • Usually reversible if normal conditions
to more hydrogen bonds restored
– Quaternary – two or more different polypeptides
interact with each other via numerous hydrogen • Irreversible if changes are extreme (high
bonds fever, severe acidosis)
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Nucleic Acids
• Composed of C, H, O, N, P
• Are the largest molecules in the body
• Nucleic acid polymers are made up of
monomers called nucleotides
• Two major classes
– Deoxyribonucleic acid (DNA)
– Ribonucleic acid (RNA)

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 Nucleic Acids Nucleic Acids
• DNA holds the genetic blueprint for the • Adenosine triphosphate (ATP) – high
synthesis of all proteins
– Double-stranded helical molecule (double helix)
energy molecule
located in cell nucleus – Chemical energy released when glucose is
– Nucleotides contain a deoxyribose sugar, broken down is captured in ATP
phosphate group, and one of four nitrogen bases:
• Purines: adenine (A), guanine (G) – ATP directly powers chemical reactions in
• Pyrimidines: cytosine (C) and thymine (T) cells
– Double-strands held together by hydrogen bonds
followed complementary base-pairing rules • Structure of ATP
• T always paired with A – Adenine-containing RNA nucleotide with two
• G always paired with C
additional phosphate groups
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Nucleic Acids
• RNA links DNA to protein synthesis and is
slightly different from DNA
– Single-stranded linear molecule is active
mostly outside nucleus
– Contains a ribose sugar (not deoxyribose)
– Thymine is replaced with uracil
– Three varieties of RNA carry out the DNA
orders for protein synthesis
• Messenger RNA (mRNA), transfer RNA (tRNA),
and ribosomal RNA (rRNA)

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